SitesBLAST
Comparing RR42_RS24965 FitnessBrowser__Cup4G11:RR42_RS24965 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
42% identity, 95% coverage: 15:379/385 of query aligns to 13:373/374 of 5lnxD
- active site: L122 (= L124), T123 (= T125), G239 (= G243), E358 (= E364), K370 (≠ R376)
- binding flavin-adenine dinucleotide: L122 (= L124), T123 (= T125), G128 (= G130), S129 (= S131), F153 (= F155), T155 (= T157), R265 (= R269), Q267 (= Q271), F268 (= F272), I272 (= I276), N275 (≠ F279), I278 (= I282), Q331 (= Q337), I332 (= I338), G335 (= G341), Y357 (= Y363), T360 (= T366), E362 (≠ Q368)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
43% identity, 95% coverage: 15:381/385 of query aligns to 10:379/379 of 6fahD
- active site: L124 (= L124), T125 (= T125), G241 (= G243), G374 (≠ R376)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), T125 (= T125), R152 (≠ T152), F155 (= F155), T157 (= T157), E198 (≠ D199), R267 (= R269), Q269 (= Q271), F270 (= F272), I274 (= I276), F277 (= F279), Q335 (= Q337), I336 (= I338), G339 (= G341), Y361 (= Y363), T364 (= T366), Q366 (= Q368)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
40% identity, 96% coverage: 9:379/385 of query aligns to 7:376/383 of 4iv6B
- active site: L121 (= L124), T122 (= T125), G240 (= G243), E361 (= E364), K373 (≠ R376)
- binding dihydroflavine-adenine dinucleotide: L121 (= L124), T122 (= T125), G126 (≠ A129), G127 (= G130), S128 (= S131), W152 (≠ F155), I153 (= I156), S154 (≠ T157), R266 (= R269), S268 (≠ Q271), F269 (= F272), I273 (= I276), H276 (≠ F279), V279 (≠ I282), R334 (≠ Q337), V335 (≠ I338), G338 (= G341), L356 (= L359), G360 (≠ Y363), T363 (= T366), E365 (≠ Q368), I366 (= I369)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 94% coverage: 18:380/385 of query aligns to 18:378/378 of 5ol2F
- active site: L124 (= L124), T125 (= T125), G241 (= G243), G374 (≠ R376)
- binding calcium ion: E29 (≠ L29), E33 (≠ T33), R35 (≠ E35)
- binding coenzyme a persulfide: L238 (= L240), R242 (= R244), E362 (= E364), G363 (= G365)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), T125 (= T125), P127 (= P127), T131 (≠ S131), F155 (= F155), I156 (= I156), T157 (= T157), E198 (≠ D199), R267 (= R269), F270 (= F272), L274 (≠ I276), F277 (= F279), Q335 (= Q337), L336 (≠ I338), G338 (= G340), G339 (= G341), Y361 (= Y363), T364 (= T366), E366 (≠ Q368)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
41% identity, 95% coverage: 13:378/385 of query aligns to 15:378/378 of 4n5fA
- active site: L126 (= L124), T127 (= T125), G243 (= G243), E364 (= E364), R376 (= R376)
- binding dihydroflavine-adenine dinucleotide: L126 (= L124), T127 (= T125), G132 (= G130), S133 (= S131), F157 (= F155), T159 (= T157), T210 (= T209), Y363 (= Y363), T366 (= T366), E368 (≠ Q368), M372 (≠ I372)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
40% identity, 98% coverage: 1:379/385 of query aligns to 5:377/379 of 1ukwB
- active site: L124 (= L124), S125 (≠ T125), T241 (≠ G243), E362 (= E364), R374 (= R376)
- binding cobalt (ii) ion: D145 (= D145), H146 (= H146)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (≠ T157), K200 (= K201), L357 (= L359), Y361 (= Y363), E362 (= E364), T364 (= T366), E366 (≠ Q368), L370 (≠ I372)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
40% identity, 98% coverage: 1:379/385 of query aligns to 5:377/379 of 1ukwA
- active site: L124 (= L124), S125 (≠ T125), T241 (≠ G243), E362 (= E364), R374 (= R376)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (≠ T157), L357 (= L359), Y361 (= Y363), E362 (= E364), T364 (= T366), E366 (≠ Q368), L370 (≠ I372)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
39% identity, 97% coverage: 11:383/385 of query aligns to 44:416/419 of Q9VSA3
- S347 (= S314) modified: Phosphoserine; by Pink1; mutation to A: Prevents phosphorylation by Pink1. Does not rescue climbing and flight defects in Pink1 mutants.; mutation to D: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.; mutation to DD: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.
7w0jE Acyl-coa dehydrogenase, tfu_1647
38% identity, 99% coverage: 1:380/385 of query aligns to 4:382/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (≠ T125), W157 (≠ F155), R270 (= R269), Q272 (= Q271), F273 (= F272), I277 (= I276), F280 (= F279), I283 (= I282), Q339 (= Q337), L340 (≠ I338), G343 (= G341), Y365 (= Y363), E366 (= E364), T368 (= T366), Q370 (= Q368), I371 (= I369)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
38% identity, 99% coverage: 1:380/385 of query aligns to 3:381/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S131), T134 (≠ A133), R180 (≠ A179), R234 (≠ K234), L237 (≠ M237), R238 (≠ K238), L240 (= L240), D241 (= D241), R244 (= R244), E365 (= E364), G366 (= G365), R377 (= R376)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), L125 (= L124), S126 (≠ T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (= T157), I360 (≠ L359), T367 (= T366), Q369 (= Q368)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
38% identity, 99% coverage: 1:380/385 of query aligns to 3:381/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ F122), L125 (= L124), S126 (≠ T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (= T157), I360 (≠ L359), Y364 (= Y363), T367 (= T366), Q369 (= Q368)
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
38% identity, 95% coverage: 14:379/385 of query aligns to 16:381/385 of 3mdeA
- active site: V125 (≠ L124), T126 (= T125), T245 (≠ G243), E366 (= E364), R378 (= R376)
- binding octanoyl-coenzyme a: T86 (≠ S84), E89 (≠ G87), L93 (≠ I92), S132 (= S131), V134 (≠ A133), S181 (= S178), F235 (= F233), M239 (= M237), F242 (≠ L240), R314 (≠ N312), Y365 (= Y363), E366 (= E364), G367 (= G365)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), V125 (≠ L124), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (= T157), R271 (= R269), T273 (≠ Q271), F274 (= F272), L278 (≠ I276), H281 (≠ F279), Q339 (= Q337), V340 (≠ I338), G343 (= G341), I361 (≠ L359), T368 (= T366), Q370 (= Q368)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
38% identity, 95% coverage: 14:379/385 of query aligns to 16:381/385 of 3mddA
- active site: V125 (≠ L124), T126 (= T125), T245 (≠ G243), E366 (= E364), R378 (= R376)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), T158 (= T157), R271 (= R269), T273 (≠ Q271), F274 (= F272), H281 (≠ F279), Q339 (= Q337), V340 (≠ I338), G343 (= G341), I361 (≠ L359), T368 (= T366), Q370 (= Q368)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
38% identity, 95% coverage: 14:379/385 of query aligns to 16:381/385 of 1udyA
- active site: V125 (≠ L124), T126 (= T125), T245 (≠ G243), E366 (= E364), R378 (= R376)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ I92), Y123 (≠ F122), S132 (= S131), S181 (= S178), F235 (= F233), M239 (= M237), F242 (≠ L240), V249 (≠ I247), R314 (≠ N312), Y365 (= Y363), E366 (= E364), G367 (= G365), I371 (= I369), I375 (= I373)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), T158 (= T157), T273 (≠ Q271), F274 (= F272), Q339 (= Q337), V340 (≠ I338), G343 (= G341), T368 (= T366), Q370 (= Q368)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
38% identity, 95% coverage: 14:379/385 of query aligns to 51:416/421 of P41367
- 158:167 (vs. 122:131, 60% identical) binding in other chain
- S167 (= S131) binding
- WIT 191:193 (≠ FIT 155:157) binding in other chain
- S216 (= S178) binding
- D278 (= D241) binding
- R281 (= R244) binding
- RKT 306:308 (≠ RKQ 269:271) binding
- HQ 316:317 (≠ FQ 279:280) binding in other chain
- R349 (≠ N312) binding
- T351 (≠ S314) binding
- QVFGG 374:378 (≠ QILGG 337:341) binding
- E401 (= E364) active site, Proton acceptor; binding
- GTAQ 402:405 (≠ GTTQ 365:368) binding in other chain
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
37% identity, 96% coverage: 14:384/385 of query aligns to 18:388/388 of 2a1tC
- active site: V127 (≠ L124), T128 (= T125), T247 (≠ G243), E368 (= E364), R380 (= R376)
- binding flavin-adenine dinucleotide: Y125 (≠ F122), V127 (≠ L124), T128 (= T125), G133 (= G130), S134 (= S131), Q155 (≠ T152), W158 (≠ F155), W158 (≠ F155), I159 (= I156), T160 (= T157), R273 (= R269), T275 (≠ Q271), F276 (= F272), L280 (≠ I276), H283 (≠ F279), I286 (= I282), Q341 (= Q337), I342 (= I338), G345 (= G341), I363 (≠ L359), T370 (= T366), Q372 (= Q368)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
37% identity, 96% coverage: 14:384/385 of query aligns to 51:421/421 of P11310
- Y67 (≠ V30) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (= L49) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (= L61) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (= L63) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ V71) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ G96) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 122:131, 60% identical) binding in other chain
- S167 (= S131) binding
- W191 (≠ F155) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (≠ FIT 155:157) binding in other chain
- T193 (= T157) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ D199) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (= D241) binding
- T280 (≠ G243) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R244) binding ; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RKQ 269:271) binding
- HQ 316:317 (≠ FQ 279:280) binding in other chain
- K329 (≠ E292) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (= QILGG 337:341) binding
- E384 (= E347) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (= E364) active site, Proton acceptor; binding ; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ EGTTQ 364:368) binding in other chain
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
39% identity, 96% coverage: 11:378/385 of query aligns to 11:376/376 of 4m9aB
- active site: L124 (= L124), T125 (= T125), G241 (= G243), E362 (= E364), R374 (= R376)
- binding dihydroflavine-adenine dinucleotide: F122 (= F122), T125 (= T125), G130 (= G130), S131 (= S131), F155 (= F155), T157 (= T157), T208 (= T209), Y361 (= Y363), T364 (= T366), E366 (≠ Q368), M370 (≠ I372)
3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr (see paper)
37% identity, 96% coverage: 10:380/385 of query aligns to 3:369/369 of 3pfdC
- active site: L116 (= L124), S117 (≠ T125), T233 (≠ G243), E353 (= E364), R365 (= R376)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F122), L116 (= L124), S117 (≠ T125), G122 (= G130), S123 (= S131), W147 (≠ F155), I148 (= I156), T149 (= T157), R259 (= R269), F262 (= F272), V266 (≠ I276), N269 (≠ F279), Q326 (= Q337), L327 (≠ I338), G330 (= G341), I348 (≠ L359), Y352 (= Y363), T355 (= T366), Q357 (= Q368)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
41% identity, 96% coverage: 11:380/385 of query aligns to 8:370/370 of 2dvlA
- active site: L121 (= L124), T122 (= T125), G233 (= G243), E354 (= E364), R366 (= R376)
- binding flavin-adenine dinucleotide: L121 (= L124), T122 (= T125), G127 (= G130), S128 (= S131), W152 (≠ F155), I153 (= I156), T154 (= T157), T356 (= T366), E358 (≠ Q368)
Query Sequence
>RR42_RS24965 FitnessBrowser__Cup4G11:RR42_RS24965
MIRDNDTLEALLDSVRRFVRERLVPAEALVAETDEIPQDIVQDMRDMGLFGMTIPERFGG
LELTMEEEVRVVMELCQTSPAFRSLLGTTVGIGSQGILMDGTPEQQAAWLPRLATGEILA
SFALTEPDAGSDAGSLRTSAIKDGDHYVVNGTKRFITNAPQAGMFTLMARTNPDIKGSAG
VSAFIVDAKTPGISFGKRDVKMGQKGAHTCDVIFENVRVPAANLIGLKEGQGFKTAMKVL
DKGRLHIAAVSVGVARRVLRDALNYALERKQFGQPISEFQLIQAMLADSQAELYAAECMV
IDAARRRDEGRNVSTEASCCKMFATEMVGRVADRAVQILGGSGYISEYGIERFYRDVRLF
RLYEGTTQIQQIIIARNMIREARDA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory